Abstract:
:We used site-directed mutagenesis to modify the Bacillus thuringiensis cry3A gene in amino acid residues 350-354. Two mutant toxins, A1 (R(345)A,Y(350)F,Y(351)F) and A2 (R(345)A,DeltaY(350), DeltaY(351)), showed significantly improved toxicity against Tenebrio molitor (yellow mealworm). The mutant toxin A1 was also more potent against both Leptinotarsa decemlineata (Colorado potato beetle) and Chrysomela scripta (cottonwood leaf beetle), while A2 displayed enhanced toxicity only in L. decemlineata. Competitive binding assays of L. decemlineata brush border membrane vesicles (BBMV) revealed that binding affinities for the A1 and A2 mutant toxins were ca. 2.5-fold higher than for the wild-type Cry3 toxin. Similar binding assays with C. scripta BBMV revealed a ca. 5-fold lower dissociation rate for the A1 mutant as compared to that of Cry3A.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Wu SJ,Koller CN,Miller DL,Bauer LS,Dean DHdoi
10.1016/s0014-5793(00)01505-2keywords:
subject
Has Abstractpub_date
2000-05-12 00:00:00pages
227-32issue
2eissn
0014-5793issn
1873-3468pii
S0014-5793(00)01505-2journal_volume
473pub_type
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